ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
A strategy for selecting the pH of protein solutions to enhance crystallization.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Fluorescence-Based Protein Stability Monitoring-A Review.International journal of molecular sciences · 2024Review
- Heterogeneous Nucleation in Protein Crystallization.Biomimetics (Basel, Switzerland) · 2023Review
- Not making the cut: Techniques to prevent RNA cleavage in structural studies of RNase-RNA complexes.Journal of structural biology: X · 2022Review
- Searching for conditions of protein self-assembly by protein crystallization screening method.Applied microbiology and biotechnology · 2021Article
- Formulation screening by differential scanning fluorimetry: how often does it work?Acta crystallographica. Section F, Structural biology communications · 2015Article
- Analysis of crystallization data in the Protein Data Bank.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Using isoelectric point to determine the pH for initial protein crystallization trials.Bioinformatics (Oxford, England) · 2015Article
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8 authors.
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Abstract
The pH of a solution is an important parameter in crystallization that needs to be controlled in order to ensure success. The actual pH of the crystallization droplet is determined by the combined contribution of the buffers in the screening and protein solutions, although the contribution of the latter to the pH is often ignored. In this study, the effects of the buffer and protein solution pH values on the results of screening are systematically investigated. It was found that these parameters significantly affected the results and thus the following strategy for the selection of appropriate pH values is proposed: (i) when screening with only one protein solution, the pH should be as low, as high or as divergent from the pI as possible for a basic, acidic or neutral protein, respectively, within its stable pH range; (ii) when screening with two protein solutions, the pH values should be well separated from one another; and (iii) when multiple pH values are utilized, an even distribution of pH values is the best approach to increase the success rate of crystallization.
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